Obstacles on the microtubule reduce the processivity of Kinesin-1 in a minimal in vitro system and in cell extract.

ABSTRACT: Inside cells, a multitude of molecular motors and other microtubule-associated proteins are expected to compete for binding to a limited number of binding sites available on microtubules. Little is known about how competition for binding sites affects the processivity of molecular motors and, therefore, cargo transport, organelle positioning, and microtubule organization, processes that all depend on the activity of more or less processive motors. Very few studies have been performed in the past to address this question directly. Most studies reported only minor effects of crowding on the velocity of motors. However, a controversy appears to exist regarding the effect of crowding on motor processivity. Here, we use single-molecule imaging of mGFP-labeled minimal dimeric kinesin-1 construct

SUBMITTER: Telley IA 

PROVIDER: S-EPMC2718299 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature